Leucine aminopeptidase

Leucine aminopeptidase (LAP) is an enzyme that catalyzes the hydrolysis of the N-terminal leucine residues from polypeptides and proteins. It is a type of exopeptidase, which are enzymes that work on the terminal residues of proteins and peptides. LAP is found in various organisms, including bacteria, plants, and animals.

Structure

Leucine aminopeptidase is a hexameric enzyme, meaning it is composed of six identical subunits. Each subunit contains a zinc ion, which is essential for the enzyme's catalytic activity. The structure of LAP is highly conserved across different species, suggesting its importance in biological processes.

Function

The primary function of leucine aminopeptidase is to remove N-terminal leucine residues from proteins and peptides. This process is crucial for protein turnover and the regulation of biological processes. In addition, LAP is involved in the processing of hormones and neuropeptides, and the degradation of abnormal or misfolded proteins.

Clinical significance

Alterations in the activity of leucine aminopeptidase have been associated with various diseases. For example, increased levels of LAP have been observed in the urine of patients with hypertension, suggesting its potential role in the pathogenesis of this condition. Furthermore, LAP inhibitors have been explored as potential therapeutic agents for the treatment of malaria, as the enzyme is essential for the life cycle of the Plasmodium parasite.

See also

• Aminopeptidase
• Exopeptidase
• Proteolysis